BMRB Entry 27523

Name: 1H, 13C, and 15N Chemical Shift Assignments for the pRN1 helix bundle domain
Published: 2019-07-10

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27523

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 13C, and 15N Chemical Shift Assignments for the pRN1 helix bundle domain

Deposition date:

2018-06-15

Original release date:

2019-07-10

Authors:

Boudet, Julien; Lipps, Georg; Allain, Frederic

Citation:

Citation: Boudet, Julien; Devillier, Jean-Christophe; Wiegand, Thomas; Salmon, Loic; Meier, Beat; Lipps, Georg; Allain, Frederic. "A small helical bundle prepares primer synthesis by binding two ATP nucleotides that enhance sequence-specific recognition of the DNA tempate" Cell ., .-..

Assembly members:

Assembly members:
free_helix_bundle_domain, polymer, 115 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Sulfolobus islandicus Taxonomy ID: 43080 Superkingdom: Archaea Kingdom: TACK group Genus/species: Sulfolobus islandicus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
free_helix_bundle_domain: TVVEFEELRKELVKRDSGKP VEKIKEEICTKSPPKLIKEI ICENKTYADVNIDRSRGDWH VILYLMKHGVTDPDKILELL PRDSKAKENEKWNTQKYFVI TLSKAWSVVKKYLEA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	370
15N chemical shifts	102
1H chemical shifts	693

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	helix bundle domain	1

Entities:

Entity 1, helix bundle domain 115 residues - Formula weight is not available

1

THR

VAL

GLU

PHE

GLU

LEU

ARG

LYS

2

GLU

LEU

VAL

LYS

ARG

ASP

SER

GLY

LYS

PRO

3

VAL

GLU

LYS

ILE

LYS

GLU

ILE

CYS

THR

4

LYS

SER

PRO

LYS

LEU

ILE

LYS

GLU

ILE

5

ILE

CYS

GLU

ASN

LYS

THR

TYR

ALA

ASP

VAL

6

ASN

ILE

ASP

ARG

SER

ARG

GLY

ASP

TRP

HIS

7

VAL

ILE

LEU

TYR

LEU

MET

LYS

HIS

GLY

VAL

8

THR

ASP

PRO

ASP

LYS

ILE

LEU

GLU

LEU

9

PRO

ARG

ASP

SER

LYS

ALA

LYS

GLU

ASN

GLU

10

LYS

TRP

ASN

THR

GLN

LYS

TYR

PHE

VAL

ILE

11

THR

LEU

SER

LYS

ALA

TRP

SER

VAL

LYS

12

LYS

TYR

LEU

GLU

ALA

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_2

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks

BMRB Entry 27523

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: